BMRB Entry 17105

Name: Solution Structure of the N-terminal Domain of NP_954075.1
Published: 2010-08-18

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PDB ID: 2l1t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17105
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the N-terminal Domain of NP_954075.1

Deposition date:

2010-08-05

Original release date:

2010-08-18

Authors:

Susac, Lukas; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Susac, Lukas; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_954075.1 from Geobacter sulfurreducens" .

Assembly members:

Assembly members:
NP_954075.1, polymer, 109 residues, 12045.543 Da.

Natural source:

Natural source: Common Name: d-proteobacteria Taxonomy ID: 35554 Superkingdom: bacteria Kingdom: not available Genus/species: Geobacter sulfurreducens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NP_954075.1: GMSADGSEYGRYFEQLQKVN LTVRLGDTGSFDGTAAITSL KGSLAWLELFGAEQPPPNTL SEGAEVSVSVWTGGALCRCD GRVETLRDDRQFAIRLVGRV RELQRREYF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	353
15N chemical shifts	113
1H chemical shifts	732

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NP_954075.1	1

Entities:

Entity 1, NP_954075.1 109 residues - 12045.543 Da.

1

GLY

MET

SER

ALA

ASP

GLY

SER

GLU

TYR

GLY

2

ARG

TYR

PHE

GLU

GLN

LEU

GLN

LYS

VAL

ASN

3

LEU

THR

VAL

ARG

LEU

GLY

ASP

THR

GLY

SER

4

PHE

ASP

GLY

THR

ALA

ILE

THR

SER

LEU

5

LYS

GLY

SER

LEU

ALA

TRP

LEU

GLU

LEU

PHE

6

GLY

ALA

GLU

GLN

PRO

ASN

THR

LEU

7

SER

GLU

GLY

ALA

GLU

VAL

SER

VAL

SER

VAL

8

TRP

THR

GLY

ALA

LEU

CYS

ARG

CYS

ASP

9

GLY

ARG

VAL

GLU

THR

LEU

ARG

ASP

ARG

10

GLN

PHE

ALA

ILE

ARG

LEU

VAL

GLY

ARG

VAL

11

ARG

GLU

LEU

GLN

ARG

GLU

TYR

PHE

Samples:

sample_1: NP_954075.1, [U-95% 13C; U-95% 15N], 0.9 mM; sodium phosphate 25 mM; sodium azide 4.5 mM; H2O 95%; H2O 5%

sample_conditions_1: ionic strength: 0.075 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (ali)	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-HACA(CO)NH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (aro)	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

UNIO, Hermann and Wuthrich - chemical shift assignment, peak picking, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2L1T
GB	AAR36425 ADI85785 AJY69279
REF	NP_954075 WP_010943660 WP_014552065